Journal
NATURE STRUCTURAL & MOLECULAR BIOLOGY
Volume 14, Issue 10, Pages 949-958Publisher
NATURE PUBLISHING GROUP
DOI: 10.1038/nsmb1292
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Funding
- NINDS NIH HHS [NS50655, NS37200, R01 NS050655, R01 NS037200] Funding Source: Medline
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Complexins constitute a family of four synaptic high-affinity SNARE complex-binding proteins. They positively regulate a late, post-priming step in Ca2+- triggered synchronous neurotransmitter release, but the underlying molecular mechanisms are unclear. We show here that SNARE complex binding of complexin I ( CplxI) via its central a-helix is necessary but, unexpectedly, not sufficient for its key function in promoting neurotransmitter release. An accessory alpha-helix on the N-terminal side of the SNARE complex-binding region has an inhibitory effect on fast synaptic exocytosis, whereas sequences N-terminally adjacent to this helix facilitate Ca2+- triggered release even in the absence of the Ca2+ sensor synaptotagmin-1. Our results indicate that distinct functional domains of CplxI differentially regulate synaptic exocytosis and that, through the interplay between these domains, CplxI carries out a crucial role in fine-tuning Ca2+- triggered fast neurotransmitter release.
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